Microsomal epoxide hydrolase of rat liver is a subunit of the anti-oestrogen-binding site

Autor: Mohamed Sebbar, Fabienne Mésange, Marc Poirot, Jean-Charles Faye, Francis Bayard, Frédéric Delarue, Joël Capdevielle, Pascual Ferrara, Jean-Claude Guillemot, Blandine Kedjouar
Přispěvatelé: Poirot, Marc, Endocrinologie et communication cellulaire, Institut Louis Bugnard-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de biochimie des proteines, Sanofi Elf-BioRecherches
Jazyk: angličtina
Rok vydání: 1998
Předmět:
MESH: Microsomes
Liver
MESH: Amino Acid Sequence
Biochemistry
Rats
Sprague-Dawley
MESH: Animals
MESH: Cycloheximide
Cloning
Molecular
Cycloheximide
Cells
Cultured
chemistry.chemical_classification
Epoxide Hydrolases
MESH: Kinetics
biology
Chemistry
Estrogen Antagonists
Affinity Labels
[SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences
Ligand (biochemistry)
Amino acid
[SDV.SP] Life Sciences [q-bio]/Pharmaceutical sciences
Liver
Microsomal epoxide hydrolase
Microsomes
Liver
Female
MESH: Cells
Cultured
Research Article
DNA
Complementary
MESH: Epoxide Hydrolases
Macromolecular Substances
Protein subunit
Affinity label
Morpholines
Ovariectomy
Molecular Sequence Data
MESH: Estrogen Antagonists
Open Reading Frames
Animals
Humans
MESH: Cloning
Molecular
RNA
Antisense
Amino Acid Sequence
Binding site
Molecular Biology
MESH: Affinity Labels
MESH: Humans
Binding Sites
MESH: Macromolecular Substances
MESH: DNA
Complementary
Cell Biology
Molecular biology
Peptide Fragments
Rats
Molecular Weight
Kinetics
Tamoxifen
MESH: Binding Sites
biology.protein
Microsome
MESH: Female
MESH: Liver
Zdroj: Biochemical Journal
Biochemical Journal, Portland Press, 1998, 334 ( Pt 1), pp.107-12
ISSN: 0264-6021
1470-8728
Popis: A tritiated photoaffinity labelling analogue of tamoxifen, [(2-azido-4-benzyl)-phenoxy]-N-ethylmorpholine (azido-MBPE), was used to identify the anti-oestrogen-binding site (AEBS) in rat liver tissue [Poirot, Chailleux, Fargin, Bayard and Faye (1990) J. Biol. Chem. 265, 17039–17043]. UV irradiation of rat liver microsomal proteins incubated with tritiated azido-MBPE led to the characterization of two photolabelled proteins of molecular masses 40 and 50 kDa. The amino acid sequences of proteolytic products from the 50 kDa protein were identical with those from rat microsomal epoxide hydrolase (mEH). Treatment of hepatocytes with anti-sense mRNA directed against mEH abolished AEBS in these cells. In addition we found that tamoxifen and N-morpholino-2-[4-(phenylmethyl)phenoxy]ethanamine, a selective ligand of AEBS, were potent inhibitors of the catalytic hydration of styrene oxide by mEH. However, functional overexpression of the human mEH did not significantly modify the binding capacity of [3H]tamoxifen. Taken together, these results suggest that the 50 kDa protein, mEH, is necessary but not sufficient to reconstitute AEBS.
Databáze: OpenAIRE
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